Fluorescence spectroscopy of osthole binding to human serum albumin

The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The...

Descripción completa

Detalles Bibliográficos
Autores principales: Yang, Guang-De, Li, Cong, Zeng, Ai-Guo, Zhao, Yuan, Yang, Rong, Bian, Xiao-Li
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Xi'an Jiaotong University 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5760984/
https://www.ncbi.nlm.nih.gov/pubmed/29403817
http://dx.doi.org/10.1016/j.jpha.2012.10.002
_version_ 1783291479641292800
author Yang, Guang-De
Li, Cong
Zeng, Ai-Guo
Zhao, Yuan
Yang, Rong
Bian, Xiao-Li
author_facet Yang, Guang-De
Li, Cong
Zeng, Ai-Guo
Zhao, Yuan
Yang, Rong
Bian, Xiao-Li
author_sort Yang, Guang-De
collection PubMed
description The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔH(0), ΔG(0) and ΔS(0) were calculated at different temperatures. The results indicated that electrostatic forces played a major role in the interaction of osthole with HSA. Results of osthole synchronous fluorescence and UV absorption spectra showed that the microenvironment and conformation of HSA were changed.
format Online
Article
Text
id pubmed-5760984
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Xi'an Jiaotong University
record_format MEDLINE/PubMed
spelling pubmed-57609842018-02-05 Fluorescence spectroscopy of osthole binding to human serum albumin Yang, Guang-De Li, Cong Zeng, Ai-Guo Zhao, Yuan Yang, Rong Bian, Xiao-Li J Pharm Anal Article The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔH(0), ΔG(0) and ΔS(0) were calculated at different temperatures. The results indicated that electrostatic forces played a major role in the interaction of osthole with HSA. Results of osthole synchronous fluorescence and UV absorption spectra showed that the microenvironment and conformation of HSA were changed. Xi'an Jiaotong University 2013-06 2012-10-23 /pmc/articles/PMC5760984/ /pubmed/29403817 http://dx.doi.org/10.1016/j.jpha.2012.10.002 Text en © 2013 Xian Jiaotong University. Production and hosting by Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Article
Yang, Guang-De
Li, Cong
Zeng, Ai-Guo
Zhao, Yuan
Yang, Rong
Bian, Xiao-Li
Fluorescence spectroscopy of osthole binding to human serum albumin
title Fluorescence spectroscopy of osthole binding to human serum albumin
title_full Fluorescence spectroscopy of osthole binding to human serum albumin
title_fullStr Fluorescence spectroscopy of osthole binding to human serum albumin
title_full_unstemmed Fluorescence spectroscopy of osthole binding to human serum albumin
title_short Fluorescence spectroscopy of osthole binding to human serum albumin
title_sort fluorescence spectroscopy of osthole binding to human serum albumin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5760984/
https://www.ncbi.nlm.nih.gov/pubmed/29403817
http://dx.doi.org/10.1016/j.jpha.2012.10.002
work_keys_str_mv AT yangguangde fluorescencespectroscopyofostholebindingtohumanserumalbumin
AT licong fluorescencespectroscopyofostholebindingtohumanserumalbumin
AT zengaiguo fluorescencespectroscopyofostholebindingtohumanserumalbumin
AT zhaoyuan fluorescencespectroscopyofostholebindingtohumanserumalbumin
AT yangrong fluorescencespectroscopyofostholebindingtohumanserumalbumin
AT bianxiaoli fluorescencespectroscopyofostholebindingtohumanserumalbumin

Ejemplares similares